{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:45:29Z","timestamp":1792784729636,"version":"4.5.0"},"reference-count":46,"publisher":"American Chemical Society (ACS)","issue":"41","license":[{"start":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:00:00Z","timestamp":1791158400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM128906"],"award-info":[{"award-number":["R35GM128906"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB-2324974"],"award-info":[{"award-number":["MCB-2324974"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Schupf Scholar Program"},{"name":"Skidmore College Faculty Student Summer Research Program","id":[{"id":"https:\/\/ror.org\/04nzrzs08","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Electrostatic interactions often play a role in determining the thermodynamic and kinetic properties of protein\u2013protein interactions. However, the role of long-range electrostatic interactions in intrinsically disordered protein (IDP) binding is less clear, as they often bind in multiple steps, including initial formation of a disordered encounter complex, followed by rearrangement into the bound state. We varied the salt concentration to probe the role of long-range electrostatic interactions in the binding of the highly charged AbpSH3 domain and the oppositely charged IDP ArkA. Using isothermal titration calorimetry, we observed that salt enthalpically destabilizes the bound complex. Molecular dynamics and NMR experiments revealed that salt has little effect on the bound state structure. However, simulations show that salt destabilizes the encounter complex intermediate, which primarily affects the association rate as measured by NMR. Consistent with these results, salt has the largest stabilizing effect on the apo SH3 domain, as cations substitute for the transient and long-range electrostatic interactions that can form with ArkA in the complex. We revealed a detailed picture of how a highly charged domain uses long-range, fuzzy, electrostatic interactions to help reach the bound state, a mechanism that is likely common among other highly charged domains that bind IDPs.<\/jats:p>","DOI":"10.1021\/acs.jpcb.6c05098","type":"journal-article","created":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T17:02:37Z","timestamp":1791219757000},"page":"10855-10872","source":"Crossref","is-referenced-by-count":0,"title":["How a Highly Acidic\nSH3 Domain Binds to Its Intrinsically\nDisordered Partner through the Formation of an Encounter Complex Intermediate"],"prefix":"10.1021","volume":"130","author":[{"given":"Valeria","family":"Jaramillo-Martinez","sequence":"first","affiliation":[{"name":"Eastern New Mexico University , , ,","place":["Portales, New Mexico, United States, 88130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ritika","family":"Kukreja","sequence":"additional","affiliation":[{"name":"University of Minnesota , , ,","place":["Minneapolis, Minnesota, United States, 55455"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michaela R.","family":"Cohen","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ally","family":"Mujica","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samuel","family":"Barton","sequence":"additional","affiliation":[{"name":"University of Liverpool , ,","place":["Liverpool, U.K., L69 7ZX"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-3193-4724","authenticated-orcid":true,"given":"Oluebube C.","family":"Onwuzulu","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]},{"name":"University of California , , ,","place":["Merced, California, United States, 95343"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge","family":"Cardoso","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew J.","family":"Dominguez","sequence":"additional","affiliation":[{"name":"Eastern New Mexico University , , ,","place":["Portales, New Mexico, United States, 88130"]},{"name":"Argonne National Laboratory , , , ,","place":["Lemont, Illinois, United States, 60439"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabelle M.","family":"Kekwick","sequence":"additional","affiliation":[{"name":"University of Liverpool , ,","place":["Liverpool, U.K., L69 7ZX"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaden","family":"Ali","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gemma M.","family":"Bell","sequence":"additional","affiliation":[{"name":"University of Liverpool , ,","place":["Liverpool, U.K., L69 7ZX"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sydney","family":"Rice","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniela","family":"Poaquiza","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Colin","family":"McClure","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]},{"name":"University of New England , , ,","place":["Biddeford, Maine, United States, 04005"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frida","family":"Anguiano","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]},{"name":"Loyola University , , ,","place":["Chicago, Illinois, United States, 60660"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2209-5798","authenticated-orcid":true,"given":"Michael P.","family":"Latham","sequence":"additional","affiliation":[{"name":"University of Minnesota , , ,","place":["Minneapolis, Minnesota, United States, 55455"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9645-555X","authenticated-orcid":true,"given":"K. Aurelia","family":"Ball","sequence":"additional","affiliation":[{"name":"Skidmore College , , ,","place":["Saratoga Springs, New York, United States, 12866"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elliott J.","family":"Stollar","sequence":"additional","affiliation":[{"name":"University of Liverpool , ,","place":["Liverpool, U.K., L69 7ZX"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,5]]},"reference":[{"key":"2026101508072267900_cit1","doi-asserted-by":"publisher","first-page":"8615","DOI":"10.3390\/ijms21228615","article-title":"Classifying\nthe Binding Modes of Disordered Proteins","volume":"21","author":"Fuxreiter","year":"2020","journal-title":"Int.\nJ. Mol. Sci."},{"issue":"10","key":"2026101508072267900_cit2","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.210222","article-title":"Intrinsically\nDisordered Proteins:\nModes of Binding with Emphasis on Disordered Domains","volume":"11","author":"Morris","year":"2021","journal-title":"Open Biol."},{"issue":"40","key":"2026101508072267900_cit3","doi-asserted-by":"publisher","first-page":"27911","DOI":"10.1074\/jbc.M114.553354","article-title":"Electrostatic Interactions in the Binding Pathway of\na Transient Protein Complex Studied by NMR and Isothermal Titration\nCalorimetry","volume":"289","author":"Meneses","year":"2014","journal-title":"J. Biol. Chem."},{"issue":"3","key":"2026101508072267900_cit4","doi-asserted-by":"publisher","first-page":"839","DOI":"10.1021\/cr800373w","article-title":"Fundamental\nAspects of Protein-Protein\nAssociation Kinetics","volume":"109","author":"Schreiber","year":"2009","journal-title":"Chem. 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Food Chem."},{"issue":"3","key":"2026101508072267900_cit20","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: A Multidimensional Spectral\nProcessing System Based on UNIX\nPipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"issue":"4","key":"2026101508072267900_cit21","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1002\/prot.20449","article-title":"The CCPN Data Model\nfor NMR Spectroscopy: Development\nof a Software Pipeline","volume":"59","author":"Vranken","year":"2005","journal-title":"Proteins: Struct., Funct.,\nBioinform."},{"issue":"19","key":"2026101508072267900_cit22","doi-asserted-by":"publisher","first-page":"5898","DOI":"10.1021\/jp074793o","article-title":"An Improved 15N Relaxation Dispersion\nExperiment for the Measurement of Millisecond Time-Scale Dynamics\nin Proteins \u2020","volume":"112","author":"Hansen","year":"2008","journal-title":"J. Phys. Chem. 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Lett."},{"issue":"10","key":"2026101508072267900_cit32","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pcbi.1002696","article-title":"Prediction and Dissection\nof Widely-Varying Association Rate Constants of Actin-Binding Proteins","volume":"8","author":"Pang","year":"2012","journal-title":"PLoS Comput. Biol."},{"issue":"13","key":"2026101508072267900_cit33","doi-asserted-by":"publisher","first-page":"6689","DOI":"10.1074\/jbc.R115.692715","article-title":"Insights into\nCoupled Folding and Binding Mechanisms from Kinetic Studies","volume":"291","author":"Shammas","year":"2016","journal-title":"J. Biol. Chem."},{"issue":"5","key":"2026101508072267900_cit34","doi-asserted-by":"publisher","first-page":"1175","DOI":"10.1016\/j.bpj.2011.06.056","article-title":"Rationalizing\n5000-Fold Differences in Receptor-Binding\nRate Constants of Four Cytokines","volume":"101","author":"Pang","year":"2011","journal-title":"Biophys. 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Biol."},{"issue":"35","key":"2026101508072267900_cit36","doi-asserted-by":"publisher","first-page":"11435","DOI":"10.1021\/bi960515w","article-title":"Alanine Point-Mutations\nin the Reactive Region of Bovine\nPancreatic Trypsin Inhibitor: Effects on the Kinetics and Thermodynamics\nof Binding to \u03b2-Trypsin and \u03b1-Chymotrypsin \u2020","volume":"35","author":"Castro","year":"1996","journal-title":"Biochemistry"},{"key":"2026101508072267900_cit37","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pcbi.1003216","article-title":"Characterizing Changes\nin the Rate of Protein-Protein\nDissociation upon Interface Mutation Using Hotspot Energy and Organization","volume":"9","author":"Agius","year":"2013","journal-title":"PLoS Comput. Biol."},{"key":"2026101508072267900_cit38","doi-asserted-by":"publisher","DOI":"10.1038\/s42003-024-06880-5","article-title":"Computational Screening\nof the Effects of Mutations on Protein-Protein off-Rates and Dissociation\nMechanisms by \u03c4RAMD","volume":"7","author":"D\u2019Arrigo","year":"2024","journal-title":"Commun. Biol."},{"key":"2026101508072267900_cit39","doi-asserted-by":"publisher","first-page":"15420","DOI":"10.1073\/pnas.1409122111","article-title":"Interplay between Partner and Ligand\nFacilitates the Folding and Binding of an Intrinsically Disordered\nProtein","volume":"111","author":"Rogers","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026101508072267900_cit40","unstructured":"A\u0301lvarez, L.; Garrone, N. A.; Claron, M.; Schweimer, K.; Glavina, J.; Will, D.; Sehr, P.; Lewis, J.; Gibson, T. J.; Sanchez, I. E.; Hennig, J.; Chemes, L. B.\n          Electrostatic Buffering of Non-Native\nInteractions in the Transition State Ensemble for Binding of Intrinsically\nDisordered Proteins. bioRxiv 2026, 06\u201323,\n2026.01.07.698246 10.64898\/2026.01.07.698246. (accessed\n2026\u201307\u201313)."},{"issue":"6","key":"2026101508072267900_cit41","doi-asserted-by":"publisher","first-page":"1313","DOI":"10.1016\/j.bpj.2018.01.031","article-title":"Molecular\nMechanisms of Tight Binding through Fuzzy\nInteractions","volume":"114","author":"Shen","year":"2018","journal-title":"Biophys. J."},{"issue":"42","key":"2026101508072267900_cit42","doi-asserted-by":"publisher","first-page":"13743","DOI":"10.1021\/bi00042a004","article-title":"Protein-Protein\nInteractions in Colicin E9 DNase-Immunity Protein Complexes. 1. Diffusion-Controlled\nAssociation and Femtomolar Binding for the Cognate Complex","volume":"34","author":"Wallis","year":"1995","journal-title":"Biochemistry"},{"key":"2026101508072267900_cit43","doi-asserted-by":"publisher","first-page":"2483","DOI":"10.1093\/nar\/gkq984","article-title":"Interpreting\nProtein\/DNA Interactions:\nDistinguishing Specific from Non-Specific and Electrostatic from Non-Electrostatic\nComponents","volume":"39","author":"Privalov","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"2026101508072267900_cit44","doi-asserted-by":"publisher","first-page":"999","DOI":"10.1006\/jmbi.1998.1738","article-title":"Calorimetric Studies\nof E. Coli SSB Protein-Single-Stranded\nDNA Interactions. Effects of Monovalent\nSalts on Binding Enthalpy","volume":"278","author":"Kozlov","year":"1998","journal-title":"J. Mol. Biol."},{"key":"2026101508072267900_cit45","doi-asserted-by":"publisher","first-page":"7570","DOI":"10.1021\/bi000377h","article-title":"Characterization\nof Sequence-Specific DNA Binding by the Transcription Factor Oct-1","volume":"39","author":"Lundba\u0308ck","year":"2000","journal-title":"Biochemistry"},{"issue":"3","key":"2026101508072267900_cit46","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1042\/EBC20200108","article-title":"Uncovering Protein Function: From\nClassification to Complexes","volume":"66","author":"Morris","year":"2022","journal-title":"Essays Biochem."}],"container-title":["The Journal of Physical\nChemistry B"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.jpcb.6c05098","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jpcbfk\/article-pdf\/130\/41\/10855\/68747064\/acs.jpcb.6c05098.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jpcbfk\/article-pdf\/130\/41\/10855\/68747064\/acs.jpcb.6c05098.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T12:29:52Z","timestamp":1792067392000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jpcbfk\/article\/130\/41\/10855\/5444654\/How-a-Highly-Acidic-SH3-Domain-Binds-to-Its"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,5]]},"references-count":46,"journal-issue":{"issue":"41","published-online":{"date-parts":[[2026,10,5]]},"published-print":{"date-parts":[[2026,10,15]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.jpcb.6c05098","relation":{},"ISSN":["1520-6106","1520-5207"],"issn-type":[{"value":"1520-6106","type":"print"},{"value":"1520-5207","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,5]]}}}